Evidence map›Paper›PMID 9621077›Full record

ArticleJournal of virology1998

Human immunodeficiency virus tat modulates the Flk-1/KDR receptor, mitogen-activated protein kinases, and components of focal adhesion in Kaposi's sarcoma cells.

R K Ganju, N Munshi, B C Nair, Z Y Liu, P Gill, J E Groopman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.2field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. HIV Associated Preeclampsia: A Multifactorial Appraisal.International journal of molecular sciences · 2021
    Review
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  18. Discovering regulated networks during HIV-1 latency and reactivation.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2006
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

R K GanjuDivisions of Experimental Medicine and Hematology/Oncology, Beth Israel Deaconess Medical Center, Harvard Institutes of Medicine, Boston, Massachusetts 02115, USA.
N Munshi
B C Nair
Z Y Liu
P Gill
J E Groopman
Beth Israel Deaconess Medical Center · USAdvanced Bioscience Laboratories (United States) · USUniversity of Southern California · US

Funding

PATHOBIOLOGY OF HIV SUPPRESSION OF HEMATOPOIESISR01HL053745 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI GROOPMAN, JEROME E · 1994 to 2004
$2.1M
THROMBOPOIETIN FOR AIDS RELATED THROMBOCYTOPOIESISR01HL055187 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI GROOPMAN, JEROME E · 1995 to 1998
–
NHLBI NIH HHS HL 43510NHLBI NIH HHS HL 53745NHLBI NIH HHS HL 55187NHLBI NIH HHS R01 HL053745
6 · The paper itself

Abstract

Kaposi's sarcoma (KS) spindle cell growth and spread have been reported to be modulated by various cytokines as well as the human immunodeficiency virus (HIV) gene product Tat. Recently, HIV-1 Tat has been shown to act like a cytokine and bind to the Flk-1/KDR receptor for the vascular endothelial growth factor A (VEGF-A), which is expressed by KS cells. We have characterized signal transduction pathways stimulated by HIV-1 Tat upon its binding to surface receptors on KS cells. We observed that stimulation in KS 38 spindle cells resulted in tyrosine phosphorylation and activation of the Flk-1/KDR receptor. We also report that HIV-1 Tat treatment enhanced the phosphorylation and association of proteins found in focal adhesions, such as the related adhesion focal tyrosine kinase RAFTK, paxillin, and p130(cas). Further characterization revealed the activation of mitogen-activated protein kinase, c-Jun amino-terminal kinase (JNK), and Src kinase. HIV-1 Tat contains a basic domain which can interact with growth factor tyrosine kinase receptors and a classical RGD sequence which may bind to and activate the surface integrin receptors for fibronectin and vitronectin. We observed that stimulation of KS cells with basic as well as RGD sequence-containing Tat peptides resulted in enhanced phosphorylation of RAFTK and activation of MAP kinase. These studies reveal that Tat stimulation activates a number of signal transduction pathways that are associated with cell growth and migration.

Indexed as

ProteinsCalcium-Calmodulin-Dependent Protein KinasesCrk-Associated Substrate ProteinCytoskeletal ProteinsFocal Adhesion Kinase 2Gene Products, tatHIV-1HumansOligopeptidesPaxillinPhosphoproteinsPhosphorylationProtein-Tyrosine KinasesReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, Vascular Endothelial Growth Factorarginyl-glycyl-aspartic acidBCAR1 protein, humanCalcium-Calmodulin-Dependent Protein KinasesCrk-Associated Substrate ProteinCytoskeletal ProteinsFocal Adhesion Kinase 2Gene Products, tatOligopeptidesPaxillinPhosphoproteinsProteinsProtein-Tyrosine KinasesPXN protein, humanReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, Vascular Endothelial Growth FactorRetinoblastoma-Like Protein p130tat Gene Products, Human Immunodeficiency VirusTyrosine

Identifiers

PMID9621077
PMCPMC110419
OpenAlexW2138012613

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.